a-ketoglutarate H + NADPH • NH, #1 NADP glatamate dehydrogenase ATP + H + NADPH ADP + NADP + P glutamate (glutamic acid) a-semialdehyde #2b elatamate kinase dehydrogenase #3 ATP + NH. #2a (spontaneous) glatamate synthetase ADP + P.+ H Text glutamine A'-pyrrolidine 5-carboxylate r + NADPH #4 NADP pyrrolidine carbaxylate reductase proline
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Are there any steps that have phosphorylation/dephosphorylation, hydration/dehydration ,or hydrolysis reactions? If so, which are they?
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- Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.Which reaction below in the glycolytic pathway has a highly unfavorable delta Gº' but a favorable delta G under physiological conditions? 1,3-Bisphosphoglycerate + ADP3-Phosphoglycerate + ATP O2-phosphoglyerate → phosphoenolpyruvate Ofructose-1,6-bisphosphate dihydroxyacetone phosphate + glyceraldehyde-3-phosphate Ofructose-6-phosphate → fructose-1,6-bisphosphate
- Discuss the metabolic rationale for phosphorylation of acetyl-CoA carboxylase by AMP-activated protein kinase (AMPK) and cyclic AMP–dependent protein kinase (PKA).Although phosphoesters are generally not energetic enough to donate the phosphate to make a high energy bond (e.g., a phosphoanhydride), the phosphate in PEP is used to convert ADP to ATP in the pyruvate kinase reaction. Carefully explain the ‘quirk’ of this reaction that makes it energetically feasible.Palmitoleic acid, 16:1Δ⁹ hexadecaenoic acid, (16 carbon FA with one double bond )is an important fatty acid component of TAGs and cell membranes. Briefly explain the process of beta oxidation of this fatty acid and the number (only) of FADH, NADH and acetyl CoA outcome. What is the total ATP (only number) generated from this fatty acid after beta oxidation.
- Trypsin uses a nearly identical mechanism as chymotrypsin (including the catalytic triad his57-ser195-asp102. beginning with the enzyme substrate complex draw the complete steps in the trypsin mechanism that occur to release the first product and create the acyl enzyme intermediate in the trypsin active site. The substrate for trypsin to be used is gly-lys-gly-ala2A. Red blood cells synthesize and degrade 2,3-bisphosphoglycerate (2,3-BPG) by a detour of the glycolytic pathway, as shown below: glyeeraldehyde 3-phosphate GAP dehydrogenase 1,3-bisphosphoglycerate bisphosphoglycerate mutase ADP phosphoglycerate kinase 2,3-bisphosphoglycerate ATP 3-phosphoglycerate 2,3-bisphosphoglycerate phosphatase phosphoglycerate mutase 2-phosphoglycerate (i) The bisphosphoglycerate mutase/2,3-bisphosphoglcerate phosphatase reaction is catalyzed by a single enzyme, BPGM. At alkaline pH, BPGM favors the mutase activity while at lower pH, BPGM favors the phosphatase reaction. Use this information, along with the Bohr effect, to explain in the space below how red blood cells respond to a metabolic defect where a patient experiences chronic, elevated levels of lactic acid. I (ii) Individuals with red blood cell phosphoglycerate kinase deficiency suffer from moderate hemolytic anemia (a condition where red blood cells self-destruct before their normal lifespan). They…The glutamate dehydrogenase (GDH) catalyses the following reaction: +H₂N- H - - CH₂ - CH₂ COO acide glutamique COO™® + NAD+ + H₂O GDH COO C: CH₂ CH₂ COO™ O + NH4+ NADH + H* The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: -0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min - Add 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start the reaction. acide a-cétoglutarique The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data: ENADH at 340 nm = 6220 M¹.cm¹ Time (min) 1 2 3 4 5 6 7 8 9 1.760 1.718 1.675 1.635 1.595 1.550 1.510 1.489 1.476 A340 10 1.451 - Draw the graph A = f(t). Calculate A340 at t = 0 and place this point on the curve. - Comment the shape of the curve, particularly the portion that corresponds to a…